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Biomedical subjects

I Pilz

Publications and source records attributed to I Pilz.

At least 55 records · Page 3Linked to original sources
PubMed1975

Small-angle x-ray studies on the structure of 16-S ribosomal RNA and of a complex of ribosomal protein S4 and 16-S ribosomal RNA from Escherichia coli.

16-S ribosomal RNA and a complex of ribosomal protein S4 and 16-S rRNA were studied in solution by small-angle X-ray scattering. Concentration series of the 16-S rRNA and the S4 - 16-S-rRNA complex were measured in 37.5 mM Tris-HCl buffer pH 7.4 at 5 degrees C. The following data were determined. The radii of gyration for the 16-S rRNA and S4 - 16-S-rRNA complex were R = 17.6 +/- 0.6 nm, respectively. The two respective values of the radii of gyration of the cross-section were Rq,1 = 8.42 +/- 0.1 nm and 8.33 +/- 0.3 nm, and Rq,2 = 0.988 +/- 0.03 nm and 0.996 +/- 0.03 nm. The largest diameters of the 16-S RNA and S4 - 16-S-RNA complex were L = 61.8 +/- 1 nm and 60.0 +/- 1 nm, respectively. Volumes of V = 1570 +/- 60 nm3 were found for both particles. In the Tris buffer used, no significant differences were found between the scattering curves of 16-S rRNA and the complex is a flat elliptical cylinder with the following dimensions: large axis 61.7 nm, small axis 35.4 nm and height 2 nm. The theoretical scattering curve fits the experimental one as long as the shape of the measured curve is due only to the overall shape of the particle. A model equivalent over the whole measured angular range is one built up from a large number of spheres that simulate the known substructure of the RNA. The outer dimensions of this model correspond to those of the flat elliptical cylinder.

Bacterial Proteins↗
PubMed1975

Shape and volume of fragments Fab' and (Fab')2 of anti-poly(D-alanyl) antibodies in the presence and absence of tetra-D-alanine as determined by small-angle x-ray scattering.

The conformation of two fragments derived from anti-poly(D-alanyl) antibodies, the divalent fragment (Fab')2 and the monovalent fragment Fab', was studied by small-angle X-ray scattering before and after interaction with the tetra-D-alanine amide hapten. More than 90% of the combining sites were occupied by the hapten. No significant changes were observed in the volume or in the radius of gyration, with either of the fragments. This contrasts with the significant decrease in these two parameters found upon reacting the hapten with intact anti-poly(D-alanyl) antibodies (I. Pilz, O. Kratky, A. Licht, and M. Sela (1973), Biochemistry 12, 4998). For Fab', the radius of the whole particle was found to be 3.48 nm in the absence of the hapten and 3.46 nm in its presence, the radius of gyration of the cross-section was 1.37 nm without hapten and 1.38 nm in its presence, and the volume of the particle was 98 nm3 in the absence of the hapten and 91 nm3 in its presence. For (Fab')2 the respective values were 5.06 and 5.05, 1.38 and 1.37, and 182 and 182. These results suggest that a conformational change occurs within the antibody molecule, but not within its Fab fragment, upon reaction with the tetraalanine hapten.

Alanine↗
PubMedDate not supplied

[Therapy and prevention in children with inflammatory rheumatic diseases].

Since 1981, annual four-week holidays have been arranged for children with juvenile rheumatic arthritis, during which the children are cared for by a team of pediatricians, orthopedists, ergotherapists, physiotherapists and assistants trained in psychology. With systematic splint therapy, physiotherapy, and by enhancing drug awareness during these therapeutic holidays significant improvements in joint mobility and subjective wellbeing were achieved. Of the 103 children treated (209 places were available), the majority spent several holidays, with a resulting improvement in joint mobility lasting several years. Through systematic training, adaptation to splints, and physiotherapy acceptance was also enhanced, with a preventive effect for the rest of the year. The success of these measures has encouraged the authors to continue the project.

Adolescent↗